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Journal of Virology, February 2000, p. 1815-1826, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Properties of the Naturally Occurring Soluble Surface Glycoprotein of Ecotropic Murine Leukemia Virus: Binding Specificity and Possible Conformational Change after Binding to Receptor

Hidetoshi Ikeda,1,* Kanako Kato,1 Takako Suzuki,1 Hiroshi Kitani,1 Yutaka Matsubara,1 Sayaka Takase-Yoden,2 Rihito Watanabe,2 Masanobu Kitagawa,3 and Shiro Aizawa4

National Institute of Animal Health, Tsukuba,1 Institute of Life Science, Soka University, Hachioji,2 Department of Pathology and Immunology, Faculty of Medicine, Tokyo Medical and Dental University, Tokyo,3 and Division of Biology and Oncology, National Institute of Radiological Sciences, Chiba,4 Japan

Received 26 July 1999/Accepted 17 November 1999

Ecotropic murine leukemia virus (MuLV) infection is initiated by the interaction between the surface glycoprotein (SU) of the virus and its cell-surface receptor mCAT-1. We investigated the SU-receptor interaction by using a naturally occurring soluble SU which was encoded by the envelope (env) gene of a defective endogenous MuLV, Fv-4r. Binding of the SU to mCAT-1-positive mouse cells was completed by 1 min at 37°C. The SU could not bind to mouse cells that were persistently infected by ecotropic MuLVs (but not amphotropic or dualtropic MuLVs) or transfected with wild-type ecotropic env genes or a mutant env gene which can express only precursor Env protein that is restricted to retention in the endoplasmic reticulum. These cells were also resistant to superinfection by ecotropic MuLVs. Thus, superinfection resistance correlated with the lack of SU-binding capacity. After binding to the cells, the SU appeared to undergo some conformational changes within 1 min in a temperature-dependent manner. This was suggested by the different properties of two monoclonal antibodies (MAbs) reactive with the same C-terminal half of the Fv-4r SU domain, including a proline-rich motif which was shown to be important for conformation of the SU and interaction between the SU and the transmembrane protein. One MAb reacting with the soluble SU bound to cells was dissociated by a temperature shift from 4 to 37°C. Such dissociation was not observed in cells synthesizing the SU or when another MAb was used, indicating that the dissociation was not due to a temperature-dependent release of the MAb but to possible conformational changes in the SU.

* Corresponding author. Mailing address: Laboratory of Virological Products, National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki-ken 305-0856, Japan. Phone: 81-298-38-7757. Fax: 81-298-38-7880. E-mail: hikeda{at}niah.affrc.go.ip.

Journal of Virology, February 2000, p. 1815-1826, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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